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Literatura académica sobre el tema "Pectin enzyme"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 9 de febrero de 2022

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Artículos de revistas sobre el tema "Pectin enzyme"

1

Pedrolli, Danielle Biscaro y Eleonora Cano Carmona. "Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation". Enzyme Research 2014 (31 de diciembre de 2014): 1–7. http://dx.doi.org/10.1155/2014/353915.

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A pectin lyase, named PLIII, was purified to homogeneity from the culture filtrate of Aspergillus giganteus grown in submerged culture containing orange peel waste as carbon source. PLIII was able to digest apple pectin and citrus pectins with different degrees of methyl esterification. Interestingly, the PLIII activity was stimulated in the presence of some divalent cations including Pb2+ and was not significantly affected by Hg2+. Like other pectin lyases, PLIII is stimulated by but is not dependent on Ca2+. The main soluble product released during the degradation of pectic substances promoted by the PLIII is compatible with an unsaturated monogalacturonate. PLIII is a unique enzyme able to release unsaturated monogalacturonate as the only soluble product during the degradation of pectic substances; therefore, PLIII was classified as an exo-pectin lyase. To our knowledge, this is the first characterization of an exo-pectin lyase. The PLIII described in this work is potentially useful for ethanol production from pectin-rich biomass, besides other common applications for alkaline pectinases like preparation of textile fibers, coffee and tea fermentation, vegetable oil extraction, and the treatment of pulp in papermaking.

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2

Chandrayan, Puja. "Biological Function(s) and Application (s) of Pectin and Pectin Degrading Enzymes". Biosciences, Biotechnology Research Asia 15, n.º 1 (25 de marzo de 2018): 87–100. http://dx.doi.org/10.13005/bbra/2611.

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Pectin is an integral part of plant cell wall and since centuries pectin extracted from plants is widely used in food and fruit juice processing. Moreover, in last half century, the applications have also invaded into many bio-processing applications such as pharmaceutical, bioenergy, textile, paper and tea processing. In these growing industries, the use of pectinases has grown with a significant amount i.e. approximately 10 % of total global enzyme market comes from pectinases. Herein comprehensive analyses of information related to structure and function of pectin in plant cell wall as well as structural classes of pectins have been discussed. The major function of pectin is in cementing the cellulose and hemicelluloses network, cell-cell adhesion and plant defence. Keeping the wide use of pectin in food industry and growing need of environment friendly technology for pectin extraction has accelerated the demand of pectin degrading enzymes (PDEs). PDEs are from three enzyme classes: carbohydrate esterases from CE8 and CE12 family, glycoside hydrolases from GH28 family and lyases from PL1, 2, 3, 9 and 10. We have reviewed the literature related to abundance and structure-function of these abovementioned enzymes from bacteria. From the current available literature, we found very limited information is present about thermostable PDEs. Hence, in future it could be a topic of study to gain the insight about structure-function of enzymes together with the expanded role of thermostable enzymes in development of bioprocesses based on these enzymes.

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3

Nakagawa, Tomoyuki, Kaichiro Yamada, Shuki Fujimura, Takashi Ito, Tatsuro Miyaji y Noboru Tomizuka. "Pectin utilization by the methylotrophic yeast Pichia methanolica". Microbiology 151, n.º 6 (1 de junio de 2005): 2047–52. http://dx.doi.org/10.1099/mic.0.27895-0.

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The methylotrophic yeast Pichia methanolica was able to grow on pectic compounds, pectin and polygalacturonate, as sole carbon sources. Under the growth conditions used, P. methanolica exhibited increased levels of pectin methylesterase, and pectin-depolymerizing and methanol-metabolizing enzyme activities. On the other hand, P. methanolica has two alcohol oxidase (AOD) genes, MOD1 and MOD2. On growth on pectin, the P. methanolica mod1Δ and mod1Δmod2Δ strains showed a severe defect in the growth yield, although the mod2Δ strain could grow on polygalacturonate to the same extent as the wild-type strain. The expression of MOD1 was detected in pectin-grown cells, but the MOD2-gene expression detected by pectin was much lower than that of MOD1. Moreover, pectin could induce peroxisome proliferation in P. methanolica, like methanol and oleic acid. These findings showed that P. methanolica was able to utilize the methylester moiety of pectin by means of methanol-metabolic enzymes in peroxisomes, and that the functional AOD subunit for pectin utilization was Mod1p in P. methanolica.

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4

Takasawa, Toshihide, Keiko Sagisaka, Koichi Yagi, Kyoko Uchiyama, Atsushi Aoki, Kyo Takaoka y Katsuhiro Yamamato. "Polygalacturonase isolated from the culture of the psychrophilic fungus Sclerotinia borealis". Canadian Journal of Microbiology 43, n.º 5 (1 de mayo de 1997): 417–24. http://dx.doi.org/10.1139/m97-059.

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A polygalacturonase was isolated from the culture medium of Sclerotinia borealis, a psychrophilic fungus that grows on lawn and wheat seedling under the snow in winter and induces the snow mold disease. Pectic acid was a better substrate of this enzyme than pectin when the activity was determined by measuring the reducing sugar produced. However, when the activity was measured by viscosity change, the viscosity of pectin decreased more rapidly than that of pectic acid. The results of viscosity change apparently indicate that the polygalacturonase catalyzes pectin hydrolysis as an endo-type enzyme. Highly methyl-esterified pectin was a poor substrate, as determined by measurements of reducing sugar production and viscosity change. It is suggested from the results that the methoxy group of pectin affects the polygalacturonase reaction. A reaction mechanism was proposed for the polygalacturonase reaction. Molecular mass of this enzyme was 40 kDa and its isoelectric point was pH 7.5. Optimum pH of the enzyme reaction was 4.5 and its optimum temperature was 40–50 °C. Thirty percent of the maximum activity was observed at 5 °C, but it was only slightly active above 60 °C. The activity was preserved for more than 2 years at 5 °C and pH 4.5, but it was lost when kept at room temperature overnight or heated at 50 °C for 30 min. The amino acid sequence of the N-terminal region of the psychrophilic polygalacturonase of Sclerotinia borealis is compared with those of polygalacturonases of mesophilic fungi. The function of this enzyme against the target plants is discussed with reference to the reaction of polygalacturonases of mesophilic fungi.Key words: polygalacturonase, pectin-hydrolyzing enzyme, psychrophilic fungi, snow mold disease, Sclerotinia borealis.

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5

Widowati, Esti, Ardhea Mustika Sari y Rokhimah Sudarmi Ningsih. "KOMBINASI ENZIM POLIGALAKTURONASE DAN ENZIM PEKTINESTERASE PADA KLARIFIKASI SARI BUAH NAGA SUPER MERAH (Hylocereus Costaricensis) DALAM PEMBUATAN SIRUP". Jurnal Teknologi Hasil Pertanian 12, n.º 1 (19 de febrero de 2020): 29. http://dx.doi.org/10.20961/jthp.v12i1.37625.

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<em>The aim of this research was to investigated the effect of polygalacturonase enzyme (PG) from Bacillus licheniformis strain GD2a AR2 0.09%, 0.1%, and 0.11% concentration combine with pectinesterase enzyme (PE) from Bacillus licheniformis strain GD2a KK2 0.5%, 1%, and 1.5% concentration on the super red dragon fruit juice calrification in syrup production based in pH, total soluble solids, transmittance, and viscosity. Polygalacturonase enzyme hydrolized the α-1,4- D-glycosidic form galacturonic acid while the pectinesterase enzyme break the metoxyl group of pectin form pectat acid. Both PG and PE work together to hydrolized pectin. Pectinesterase catalyzed pectin become pectat acid as the substrat for polygalacturonase. In the lower acid degree, polygalcturonase and pectinesterase enzyme combination cause the viscosity and total soluble solids decrease. Degradation of pectin cause the transmittance of super red dragon fruit syrup increase. The result of this research were obtained a partially pure polygalacturonase enzyme with enzyme activity 0.31 U/ml while the pectinesterase enzyme activity was 1.167 U/ml. Samples with the addition 0.11% concentration of poligalakturonase enzyme and 0.5% concentration of pectinesterase enzyme with pH value of 4.303, total soluble solid value of 38.133<sup>o</sup>Brix, transmittance value of 74.5%T, and viscocity value of 0.128cP was selected sample. </em>

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6

Fissore, E. N., N. M. Ponce, C. A. Stortz, A. M. Rojas y L. N. Gerschenson. "Characterisation of Fiber Obtained from Pumpkin (cucumis moschata duch.) Mesocarp Through Enzymatic Treatment". Food Science and Technology International 13, n.º 2 (abril de 2007): 141–51. http://dx.doi.org/10.1177/1082013207077914.

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Cell wall-enriched pumpkin ( Cucumis moschata Duch.) powder was submitted to enzymatic hydrolysis by cellulase or hemicellulase in order to evaluate the performance of these cell wall-degrading enzymes on that substrate. Different enzyme-substrate ratios were evaluated and the effect exerted by the buffer on cell wall polysaccharides. Cellulase produced the release of pectin macromolecules which include homogalacturonans side chains, the rhamnogalacturonan I core and rhamnogalacturonan II, in conjunction with xylogalacturonans. The content of galacturonic acid in product obtained ranged from 545 to 781 g/kg of fiber. Hemicellulases produced intense pectin hydrolysis leading to fiber-fractions with galacturonic acid contents ranging from 390 to 444 g/kg of fiber and enriched in glucose polymers as the enzyme proportion increased. Few rhamnogalacturonan-I was present.The acidic citrate buffer (pH 5.2) used for allowing enzyme activity could per se remove noncovalent cross-links like ionic bonds. As a consequence, pectin-in-extensin entanglements, pectins joined by Ca2+-bridges through the homogalacturonan side chains, and some pectins that are originally soluble in cold water due to little or no binding to the cell wall, could be removed by this citrate buffer. Enzymatic hydrolysis as well as buffer extraction produced fiber-products with an important thickening effect of aqueous systems. This effect was smaller as the ratio enzyme-substrate was increased and, in general, the fiber fractions isolated produced an in vitro glucose diffusion retardation.

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7

Leone, G. y J. Van den Heuvel. "Regulation by carbohydrates of the sequential in vitro production of pectic enzymes by Botrytis cinerea". Canadian Journal of Botany 65, n.º 10 (1 de octubre de 1987): 2133–41. http://dx.doi.org/10.1139/b87-294.

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Cultures of Botrytis cinerea in a basal salt medium supplemented with different pectin-related polysaccharides (French bean cell walls; citrus pectin; sodium polygalacturonate) as the only carbon source were examined daily for polygalacturonase activity, type of pectic enzymes present, and mycelial growth. Total polygalacturonase activity and number of enzymes detectable were influenced by type and concentration of the substrate and by the conidial concentration at which the cultures were started. A consistent sequence in the production of pectic enzymes was found. The polygalacturonase PG2 was always the first enzyme present in the culture filtrates and was followed by a number of polygalacturonase and pectinesterase isoenzymes. PG2 was also found in ungerminated conidia. Its production is the expression of a constitutive gene as it was independent of the presence of the substrate and strictly correlated with fungal growth. D-Galacturonic acid at 2 mM induced the production of some of the pectic enzymes. At 10 mM and above, however, it repressed PG2 and the subsequent production of the whole pectic isoenzyme complex, indicating a feedback repression. The results suggest that the pectic isoenzymes produced by B. cinerea constitute a coordinated catabolic pathway for the complete degradation of pectic polysaccharides.

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8

Huang, Cian-Song, Qiao-Lin Li, Diana Lo, Yuh-Tai Wang y Ming-Chang Wu. "Anti-inflammatory activity of pectic enzyme-treated pectin on lipopolysaccharide-induced RAW 264.7 cells". Journal of Functional Food and Nutraceutical 1, n.º 1 (21 de agosto de 2019): 23–30. http://dx.doi.org/10.33555/jffn.v1i1.14.

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The purpose of this study was to investigate the ability and pathway of the pectic enzyme-treated (PET) pectin to inhibit the inflammation of macrophage RAW 264.7 induced by lipopolysaccharide. Results showed that PET-pectin produced from 1% substrate and 48 h reaction time had the highest antioxidative activity, thus these parameters were used to produce PET-pectin used in this study. PET-pectin showed no cell cytotoxicity to normal macrophage RAW 264.7 and reduce the nitrite secretion from LPS-induced RAW 264.7 by 20%. Finally, the expression of cytokines, including NO synthase (iNOS), nitric oxide (NO), cyclooxygenase-2 (COX-2), nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and tumor necrosis factor (TNF-α) were analyzed by western blot. In the western blot method, it was found that iNOS, COX-2, NF-κB, TNF-α and other proteins that activated NO production had a downtrend. It was found that PET-pectin possess promising activity to mitigate the inflammatory response.

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9

Yuan, Ye, Xin-Yu Zhang, Yan Zhao, Han Zhang, Yi-Fa Zhou y Juan Gao. "A Novel PL9 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Its Application in Pectin Degradation". International Journal of Molecular Sciences 20, n.º 12 (22 de junio de 2019): 3060. http://dx.doi.org/10.3390/ijms20123060.

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Pectate lyases play an important role in pectin degradation, and therefore are highly useful in the food and textile industries. Here, we report on the cloning of an alkaline pectate lyase gene (pppel9a) from Paenibacillus polymyxa KF-1. The full-length gene (1350 bp) encodes for a 449-residue protein that belongs to the polysaccharide lyase family 9 (PL9). Recombinant PpPel9a produced in Escherichia coli was purified to electrophoretic homogeneity in a single step using Ni2+-NTA affinity chromatography. The enzyme activity of PpPel9a (apparent molecular weight of 45.3 kDa) was found to be optimal at pH 10.0 and 40 °C, with substrate preference for homogalacturonan type (HG) pectins vis-à-vis rhamnogalacturonan-I (RG-I) type pectins. Using HG-type pectins as substrate, PpPel9a showed greater activity with de-esterified HGs. In addition, PpPel9a was active against water-soluble pectins isolated from different plants. Using this lyase, we degraded citrus pectin, purified fractions using Diethylaminoethyl (DEAE)-sepharose column chromatography, and characterized the main fraction MCP-0.3. High-performance gel permeation chromatography (HPGPC) analysis showed that the molecular mass of citrus pectin (~230.2 kDa) was reduced to ~24 kDa upon degradation. Ultra-performance liquid chromatography - tandem mass spectrometer (UPLC-MS) and monosaccharide composition analyses demonstrated that PpPel9a worked as an endo-pectate lyase, which acted primarily on the HG domain of citrus pectin. In vitro testing showed that the degradation product MCP-0.3 significantly promotes the growth of Lactobacillus plantarum and L. rhamnosus. In this regard, the enzyme has potential in the preparation of pharmacologically active pectin products.

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10

Pieczywek, Piotr Mariusz, Justyna Cybulska y Artur Zdunek. "An Atomic Force Microscopy Study on the Effect of β-Galactosidase, α-l-Rhamnosidase and α-l-Arabinofuranosidase on the Structure of Pectin Extracted from Apple Fruit Using Sodium Carbonate". International Journal of Molecular Sciences 21, n.º 11 (5 de junio de 2020): 4064. http://dx.doi.org/10.3390/ijms21114064.

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The enzyme driven changes in plant cell wall structure during fruit ripening result in debranching, depolymerization and solubilization of pectin polysaccharides, which has an effect in terms of the postharvest quality losses in fruit. Atomic force microscopy (AFM) has revealed that diluted alkali soluble pectins (DASP) from fruit and vegetables have an interesting tendency to self-assemble into regular structures. However, the mechanism is not yet fully understood. The current study is aimed at investigating the role of neutral sugars, namely galactose, rhamnose and arabinose in the formation of the branched structure of DASP. β-galactosidase, α-l-rhamnosidase and α-l-arabinofuranosidase enzymes were used for the treatment of DASP extracted from Golden Delicious apple flesh (Malus domestica cv. Golden Delicious). The effects of the selective degradation of pectic polysaccharides after 15, 30, 60, 90 and 120 min of incubation were observed using AFM. The α-l-rhamnosidase enzyme activity on pectin extracted with Na2CO3 did not cause any visible or measurable degradation of the molecular structure. The moderate effects of β-galactosidase enzymatic treatment suggested the possible role of galactose in the branching of DASP molecules deposited on mica. Data obtained for α-l-arabinofuranosidase indicated the crucial role of arabinose in the formation and preservation of the highly branched structure of the DASP fraction.

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Tesis sobre el tema "Pectin enzyme"

1

Barnby, F. M. "An investigation of the pectinolytic enzyme system of Kluyveromyces marxianus". Thesis, University of Reading, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.378305.

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2

Larsson, Malin y Annie Nilsson. "Förädling av stjälkfibrer för fler naturliga fiberalternativ : Enzymbehandling för avlägsnande av pektin i stjälkfibrer för ökad spinnbarhet". Thesis, Högskolan i Borås, Akademin för textil, teknik och ekonomi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:hb:diva-295.

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Grewia optiva är en utav många outnyttjade stjälkfibrer som skulle kunna bidra till ökandet utav de naturliga fiberalternativen. Fibern har idag inte så många användningsområden på grund utav dess hårda och styva uppbyggnad, vilket gör den svår att spinna till garn. På uppdrag av organisationen Bhartiya Gramotthan Sanstha (BGS) har i detta projekt en redan befintlig metod utvecklats för att förädla fibern. Vad som främst eftersöktes var nedbrytandet av pektin som är en av de faktorer som bidrar till fiberns hårda och styva struktur. I metoden användes biologiskt nedbrytbara enzym som katalysatorer. En fungerande metod skulle kunna öka användningsområdet hos stjälkfibrer generellt och öka möjligheten till användandet utav fler naturliga fibrer. Enzymet som har använts i metoden är ett pektatlyas EC 4.2.2.2 som katalyserar reaktionen som sker då pektinmolekyler klyvs. För att effektivisera processen adderades en komplexbildare, EDTA, som tidigare visat goda resultat för lin. Efter enzymbehandlingen skedde en viktreduktion av fibrerna samt förändring av deras utseende. I svepelektronmikroskop observerades förändring av ytstruktur samt separation mellan fiberbuntarna. Dessa parametrar är viktiga och har stor inverkan på spinnbarheten hos fibrer. I projektet har försök att spinna fibern gjorts men inte lyckats helt. Förändringen på ytstruktur och separation mellan fibrerna tyder dock på att behandlingen är ett steg i rätt riktning.
Grewia optiva is one of many unused bast fibres that could contribute to an increase of natural textile fibres on the industrial market. This fibre has to-day not as many applications due to its stiff and hard structure that makes the fibre difficult to spin into yarn. On behalf of the organisation Bhartiya Gramotthan Sanstha (BGS) has an existing method been developed to process the Grewia optiva fibre. The method is developed to break down substances like pectin that is responsi-ble for the hard and stiff structure of the fibre. Degradable biological en-zymes were used as catalyser in the method. With a functioning method like this the applications of bast fibres could increase and contribute to the use of more natural fibres. The enzyme used to catalyse the chemical reaction and the cleavage of pec-tin molecules in this method was a pectate lyase EC 4.2.2.2. In this method EDTA was used as a chelator to efficient the chemical process. EDTA has been used as a chelator in earlier reports and showed good results. After the enzymatic treatment a weight reduction of the fibre was notable. In SEM-analysis separation between fibres and changes on the fibre surfaces was observed. These parameters are important and affect the spinning capability of the fibre. To test the spinning capability of the enzyme treated fibre they were spun in a ring spinning system, unfortunately not successfully. The surface changes and the separation shows that the enzymatic treatment had occurred and indicates that the method has developed in the right direction.

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3

Takeya, Tomoyuki. "Synthetic biological studies on production of methanol from natural resource-derived carbon compounds". Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263712.

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Ali, Ahmed. "Use of pectinases to improve the nutritive value of lupins for poultry". University of Western Australia. School of Animal Biology, 2009. http://theses.library.uwa.edu.au/adt-WU2010.0094.

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[Truncated abstract] Australia produces 87% of the worlds lupins (Lupinus angustifolius) which have the potential to be an excellent source of protein and energy in animal diets. However, feed manufacturers and poultry producers cannot use more than about 5% lupins in broiler and 7% in layer diets. The main reason is because 34% of the lupin grain comprises complex cell-wall polysaccharides that are indigestible. The main component of cell walls in lupins is pectin (33%). Poultry cannot digest pectin because they don't secrete the appropriate enzymes so their ability to use lupins is limited. Undigested pectins increase the viscosity of digesta in the bird's digestive tract, which in turn reduces the digestibility of dry matter and efficiency of feed utilisation. Pectins also increase water-holding capacity, a characteristic directly related to water intake and wet droppings. In this thesis, I tested the general hypothesis that breakdown of cell walls and pectins will improve the nutritive value of lupins for broilers and layers and reduce wet droppings. This hypothesis was tested in six experiments by treating lupins with specific exogenous enzymes (pectinases) or mechanical-heat treatment (expansion) plus pectinase. In the first experiment, attempts to break down the cell walls and pectins using four doses of pectinase, specifically polygalacturonase (PG), succeeded in improving the nutritive value of whole and dehulled lupins for egg layers. The lowest dose, 0.6g/kg diet, was the most effective dose for reducing water intake, wet droppings, the viscosity of the digesta and the number of soiled eggs. ... Equivalent figures for layers were 14, 15, 5 and 8%, indicating that the pectinases were slightly more effective in layers than broilers. For diets containing 20% dehulled lupins, pectinases were also very effective at breaking down both pectin and cell walls to release nutrients and, concomitantly, reducing water intake and wet droppings, but the magnitude of the responses was slightly less than with the 10% dehulled lupin diets. For diets containing 30% dehulled lupins, although the pectinases again were effective at breaking down pectin and cell walls and reducing viscosity, they did not reduce water intake or wet droppings. This might be due to the large amounts of nonmethylated pectic polysaccharides, which make up two thirds of the cell walls, by increasing water-holding capacity particularly when dehulled lupins are included in the diet at high levels (up to 30%). These polysaccharides might be broken down by appropriate enzymes. This hypothesis is worth testing in the future. Overall, the results of my study supported the general hypothesis. These in vivo results are conclusive and consistent. They show that an optimum combination of PME and PG is capable of including dehulled lupins up to 20% in broiler and layer diets without any nutritional or hygienic problems. The strategies I developed have proven very useful for breaking down the cell walls and pectins, improving the nutritive value of lupins for broilers and layers, and reducing wet droppings. By using the optimum combination of two pectinases, it should be possible to make substantial improvements in the nutritive value of lupins for broilers and layers, most importantly by reducing excessive water intake and wet droppings associated with feeding dehulled lupins. Without pectinases, the amount of dehulled lupins used in poultry diets is fairly small (7%), but if pectinases are used, this upper limit can be lifted to 20%.

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5

Massiot, Patrice. "Caracterisation structurale et degradation enzymatique des polysaccharides de parois cellulaires de la racine de carotte (daucaus carota l. )". Rennes 1, 1988. http://www.theses.fr/1988REN10089.

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McKie, Vincent Arthur. "The isolation and characterisation of pectin degrading enzymes". Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287822.

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Legentil, Anne. "Étude de la composition chimique des pectines de la paroi cellulaire de la fraise et de leur solubilisation par des préparations enzymatiques industrielles : application à la liquéfaction de la fraise". Vandoeuvre-les-Nancy, INPL, 1996. http://www.theses.fr/1996INPL018N.

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Le procédé de liquéfaction des fruits, nécessite l'emploi d'enzymes pectinolytiques, considérées comme des auxiliaires technologiques. L’optimisation de l'hydrolyse enzymatique passe par une meilleure connaissance de la paroi cellulaire du fruit. La paroi cellulaire de la fraise a été isolée du fruit par une extraction à l'alcool. Le matériel ainsi obtenu (MIA) a été soumis à des extractions successives par l'acide trans-1,2-diamino-cyclohexane-n,n,n',n'-tétraacétique, un tampon succinate pH 4,8, l'acide chlorhydrique dilué à chaud et la soude diluée à froid. L’analyse des différents extraits a permis de montrer que 87% des pectines solubles de la fraise sont extractibles par un agent chélatant du calcium (CDTA). Ces pectines sont faiblement méthylées et peu ramifiées. Les pectines les plus ramifiées nécessitent des conditions d'extraction plus drastiques (HCl et NaOH dilués). Le fractionnement par chromatographie échangeuse d'ions a permis de montrer que certaines fractions pectiques sont riches en oses neutres pouvant provenir des hémicelluloses (xylose, glucose), et en protéines. Les résultats obtenus permettent de suspecter la présence de liaisons entre les pectines, les hémicelluloses et les protéines au sein de la paroi cellulaire. La liquéfaction de la paroi (MIA) et de l'extrait insoluble dans le CDTA à l'aide d'enzymes industrielles a mis en évidence, outre la synergie entre les activités pectinolytiques et cellulolytiques, l'importance des activités hémicellulolytiques et protéolytiques. Ces études ont permis de mettre au point une nouvelle formulation enzymatique permettant d'améliorer le rendement d'extraction du jus et d'optimiser la stabilité des anthocyanes (couleur) au cours du stockage. En outre, cette étude a montré l'effet néfaste de la pasteurisation et de la concentration sur la couleur des jus

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8

Şimşek, Şebnem Yemenicioğlu Ahmet. "Production of commercially suitable pectin methylesterase and polyphenol oxidase from agro-industrial wastes/". [s.l.]: [s.n.], 2004. http://library.iyte.edu.tr/tezler/master/gidamuh/T000508.doc.

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9

Faraj, K. A. "A study of pectic substances and their enzymic degradation". Thesis, University of Strathclyde, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.372091.

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10

Miyawaki, Miyuki. "Control of polyphenol oxidase and pectin methylesterase activities by ultra high pressure". Online access for everyone, 2006. http://www.dissertations.wsu.edu/Dissertations/Spring2006/M%5FMiyawaki%5F033106.pdf.

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Más fuentes

Libros sobre el tema "Pectin enzyme"

1

Buell, Carol Robin. The role of pectic enzymes in the Fusarium solani -pea endocarp system. 1988.

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Capítulos de libros sobre el tema "Pectin enzyme"

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Schomburg, Dietmar y Margit Salzmann. "Pectin lyase". En Enzyme Handbook 1, 943–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_212.

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Dongowski, G., S. Förster y H. Kunzek. "Effect of Pectolytic and Cellulolytic Enzyme Treatments on Functional and Nutritional Properties of Cell Wall Materials from Apples". En Advances in Pectin and Pectinase Research, 491–504. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0331-4_36.

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Bonnin, Estelle y Jérôme Pelloux. "Pectin Degrading Enzymes". En Pectin: Technological and Physiological Properties, 37–60. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-53421-9_3.

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Lineweaver, Hans y Eugene F. Jansen. "Pectic Enzymes". En Advances in Enzymology - and Related Areas of Molecular Biology, 267–95. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122563.ch5.

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Wong, Dominic W. S. "Pectic Enzymes". En Food Enzymes, 212–36. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2349-6_7.

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Tazawa, Kenji, Hideo Okami, Iwao Yamashita, Yasuharu Ohnishi, Kyoichi Kobashi y Masao Fujimaki. "Effects of Apple Pectin on Fecal Enzyme Activities and Prostaglandin E2 Levels in Azoxymethane-induced Rat Colon Carcinogenesis". En Food Factors for Cancer Prevention, 178–81. Tokyo: Springer Japan, 1997. http://dx.doi.org/10.1007/978-4-431-67017-9_36.

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Deuel, H. y E. Stutz. "Pectic Substances and Pectic Enzymes". En Advances in Enzymology - and Related Areas of Molecular Biology, 341–82. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122655.ch11.

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Tazawa, Kenji, Hideo Ookami, Iwao Yamashita, Tetsuro Shimizu, Masao Fujimaki, Kenji Murai, Kyoichi Kobashi y Takashi Honda. "Effect of Apple Pectin on Azoxymethane-Induced Colon Carcinogenesis — Fecal Enzyme Activities and Prostaglandin E2 Level in Colonic Mucosa". En Recent Advances in Management of Digestive Cancers, 471–73. Tokyo: Springer Japan, 1993. http://dx.doi.org/10.1007/978-4-431-68252-3_132.

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Kalamaki, Mary S., Nikolaos G. Stoforos y Petros S. Taoukis. "Pectic Enzymes in Tomatoes". En Food Biochemistry and Food Processing, 232–46. Oxford, UK: Wiley-Blackwell, 2012. http://dx.doi.org/10.1002/9781118308035.ch12.

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Hartzell, M. Michelle y You-Lo Hsieh. "Pectin-Degrading Enzymes for Scouring Cotton". En ACS Symposium Series, 212–27. Washington, DC: American Chemical Society, 1998. http://dx.doi.org/10.1021/bk-1998-0687.ch018.

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Actas de conferencias sobre el tema "Pectin enzyme"

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Mikkelsen, Jorn Dalgaard, Paul Knox, Bill Willats y Tove M. I. E. Christensen. "STRUCTURE-FUNCTIONALITY OF PECTIN AND PECOLYTIC ENZYMES". En XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.790.

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Kasakova, A. S., I. S. Tatyanchenko, L. A. Kuleshova y A. F. Tatyanchenko. "COMPARATIVE EVALUATION OF SPRING BARLEY VARIETIES BY AMYLASE ACTIVITY IN GERMINATING SEEDS". En STATE AND DEVELOPMENT PROSPECTS OF AGRIBUSINESS. DSTU-PRINT, 2020. http://dx.doi.org/10.23947/interagro.2020.1.147-150.

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A comparative study of the activity of amylolytic enzymes of six varieties of spring barley grown in the Educational and experimental farm of the Azov-black sea engineering Institute in two different hydrothermal conditions of the year (moderate arid and arid). It was proposed to compare the activity of these enzymes in four microphenophases: dry grain, pecking, fork and sprout for a comparative mass evaluation of all varieties. Quantitative differences in micropenises, by grade and year of reproduction.

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Widmer, Wilbur, Weiyang Zhou y Karel Grohmann. "Converting Citrus Waste to Ethanol and Other Co-Products". En ASME 2009 Citrus Engineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/cec2009-5502.

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Conversion of citrus processing waste (CPW) generated during juice production into value added co-products is an important aspect of the juice industry as it offers a solution to waste disposal issues. Currently the practice of drying citrus waste to produce citrus pulp pellets (CPP) for use as cattle feed is profitable. However, until the recent rise in value, CPP value was marginal and often did not meet production costs. Another concern has been volatile organic emissions during CPP production. Only one third of the residual peel oil present in citrus waste is recovered during CPP production with most being vented to the atmosphere during drying and is a growing environmental concern. Improvements in limonene recovery and development of alternative value added co-products obtained from CPW could add substantial value to the citrus crop. For current CPP production, the energy required to dry CPW is the major cost involved and approximately 25 lb of limonene are obtained per ton of CPP produced. Since limonene is recovered during evaporation/concentration of pressed peel juice using a waste heat evaporator, little additional cost is associated with limonene recovery. The concentrated citrus molasses produced may be added back to the press cake or fermented to make ethanol, but only contains a third of the sugars in CPW that are fermentable by conventional yeast. While utilizing the entire CPW stream for ethanol using hydrolysis and fermentation is more involved, three times the amount of ethanol can be obtained compared to using press liquor alone. Most of the limonene must be removed as it inhibits fermentation. In the process developed 85–95% of the limonene contained in CPW can be removed and recovered by steam stripping. This greatly reduces concerns associated with the release of volatile organic compounds (VOCs) during processing of CPW and the limonene recovered has a value equal or greater than stripping costs. Using a mixture of enzymes and yeast, the CPW is then hydrolyzed and fermented simultaneously to produce ethanol followed by distillation to remove and recover the ethanol. Enzyme costs to hydrolyze and liquefy CPW have been reduced to less than a dollar per gallon of ethanol produced, and the economics for distillation are still being optimized. The distillation residues contain half the solids of raw citrus waste that can still be utilized as a CPP product. Other uses for the residues such as incorporation of the pectic materials into building product and paper additives, and ion exchange materials for wastewater remediation are also in development. Paper published with permission.

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